1epa: Difference between revisions

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1epa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1epa OCA], [http://www.ebi.ac.uk/pdbsum/1epa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1epa RCSB]</span>
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[[Category: retinoic acid-binding protein]]
[[Category: retinoic acid-binding protein]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:58:38 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:07:05 2008''

Revision as of 20:07, 30 March 2008

File:1epa.gif


PDB ID 1epa

Drag the structure with the mouse to rotate
, resolution 2.1Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF THE EPIDIDYMAL RETINOIC ACID-BINDING PROTEIN AT 2.1 ANGSTROMS RESOLUTION


OverviewOverview

BACKGROUND: Androgen-dependent proteins in the lumen of the epididymis are required for sperm maturation. One of these is a retinoic acid binding protein, E-RABP, which binds both all-trans and 9-cis retinoic acid. The other retinoid-binding proteins whose structures are known do not bind 9-cis retinoids. RESULTS: We describe the X-ray structure determination of E-RABP with and without bound ligand. The ligand binds deep in the beta-barrel of the protein, the beta-ionone ring innermost. The binding site, like the ligand, is amphipathic and the deepest part of the cavity is formed by a ring of aromatic amino acids. The isoprene tail of all-trans retinoic acid is bound in a folded conformation which resembles that of the 9-cis isomer. CONCLUSION: E-RABP achieves high-affinity binding of both all-trans and 9-cis isomers of retinoic acid by forcing the all-trans form to bind in a folded conformation. The RAR family of nuclear receptors for retinoic acid also binds both isomers, and their binding sites may therefore be similar.

About this StructureAbout this Structure

1EPA is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the epididymal retinoic acid binding protein at 2.1 A resolution., Newcomer ME, Structure. 1993 Sep 15;1(1):7-18. PMID:8069623

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